Evidence map›Paper›PMID 24741044›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2014

Myocilin is involved in NgR1/Lingo-1-mediated oligodendrocyte differentiation and myelination of the optic nerve.

Heung Sun Kwon, Naoki Nakaya, Mones Abu-Asab, Hong Sug Kim, Stanislav I Tomarev

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 35 citations in OpenAlex.

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  12. Ancestry-specific and sex-specific risk alleles identified in a genome-wide gene-by-alcohol dependence interaction study of risky sexual behaviors.American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics · 2017
    Article
  13. Myocilin Regulates Metalloprotease 2 Activity Through Interaction With TIMP3.Investigative ophthalmology & visual science · 2017
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Heung Sun KwonRetinal Ganglion Cell Biology Section, Laboratory of Retinal Cell and Molecular Biology and Histology Core, National Eye Institute, National Institutes of Health (NIH), Bethesda, Maryland 20892, and Neuro-Oncology Branch, National Cancer Institute, NIH, Bethesda, Maryland 20892.
Naoki Nakaya
Mones Abu-Asab
Hong Sug Kim
Stanislav I Tomarev
National Cancer Institute · USNational Eye Institute · USNational Institutes of Health · US

Funding

Molecular Mechanisms Of GlaucomaZIAEY000318 · NEI · NATIONAL EYE INSTITUTE · PI TOMAREV, STANISLAV I · 2009 to 2025
$18.9M
Intramural NIH HHS
6 · The paper itself

Abstract

Myocilin is a secreted glycoprotein that belongs to a family of olfactomedin domain-containing proteins. Although myocilin is detected in several ocular and nonocular tissues, the only reported human pathology related to mutations in the MYOCILIN gene is primary open-angle glaucoma. Functions of myocilin are poorly understood. Here we demonstrate that myocilin is a mediator of oligodendrocyte differentiation and is involved in the myelination of the optic nerve in mice. Myocilin is expressed and secreted by optic nerve astrocytes. Differentiation of optic nerve oligodendrocytes is delayed in Myocilin-null mice. Optic nerves of Myocilin-null mice contain reduced levels of several myelin-associated proteins including myelin basic protein, myelin proteolipid protein, and 2'3'-cyclic nucleotide 3'-phosphodiesterase compared with those of wild-type littermates. This leads to reduced myelin sheath thickness of optic nerve axons in Myocilin-null mice compared with wild-type littermates, and this difference is more pronounced at early postnatal stages compared with adult mice. Myocilin also affects differentiation of oligodendrocyte precursors in vitro. Its addition to primary cultures of differentiating oligodendrocyte precursors increases levels of tested markers of oligodendrocyte differentiation and stimulates elongation of oligodendrocyte processes. Myocilin stimulation of oligodendrocyte differentiation occurs through the NgR1/Lingo-1 receptor complex. Myocilin physically interacts with Lingo-1 and may be considered as a Lingo-1 ligand. Myocilin-induced elongation of oligodendrocyte processes may be mediated by activation of FYN and suppression of RhoA GTPase.

Indexed as

Age FactorsAnimalsAnimals, NewbornCell DifferentiationCells, CulturedChlorocebus aethiopsCytoskeletal ProteinsEye ProteinsFemaleGanglia, SpinalGene Expression RegulationGlycoproteinsGPI-Linked ProteinsHumansIn Vitro TechniquesMaleCytoskeletal ProteinsEye ProteinsGlycoproteinsGPI-Linked ProteinsLINGO1 protein, humanMembrane ProteinsMyelin ProteinsMyocilinNerve Tissue ProteinsNogo Receptor 1Receptors, Cell SurfaceRTN4R protein, humanastrocytedifferentiationLingo-1myelinmyocilinoligodendrocyte

Identifiers

PMID24741044
PMCPMC3988410
OpenAlexW2000071829

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.